University of North Florida
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Stuart Chalk, Ph.D.
Department of Chemistry
University of North Florida
Phone: 1-904-620-1938
Fax: 1-904-620-3535
Email: schalk@unf.edu
Website: @unf

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Ikuo Satoh

Abbrev:
Satoh, I.
Other Names:
Address:
Department of Applied Chemistry, Faculty of Engineering, Kanagawa Institute of Technology, 1030 Shimo-Ogino, Atsugi, Kanagawa-ken 243-0292, Japan
Phone:
+81-46-291-3105
Fax:
+81-46-291-3105

Citations 13

"Thermolysin As A Recognition Element For Microdetermination Of Zinc(II) Ions Based On The Apoenzyme Reactivation Methods"
Trans. 2001 Eurosens. XV 2001 Volume 2, Issue 1 Pages 1262-1265
Ikuo Satoh, Tsuyoshi Ishigami, Sayaka Oyanagi and Yasuhiro Iida

Abstract: A spectrophotometric flow injection analysis (FIA) with a column containing thermolysin-immobilized glass beads was applied to microdetermination of zinc(II) ions based on the apoenzyme reactivation method. The catalytic activity of the enzyme-packed column was assessed by injecting 1.0 mL of synthetic oligopeptide solution as a substrate into the system. The column was regenerated on exposure to 100 mM EDTA solution and reversibly reactivated with addition of zinc(II) ions. Thus, zinc(II) ions in a range of 1.0 nM to 5.0 mM were determined. [Conference Paper; 9 Refs]

"Fluorometric Determination Of Urea In Alcoholic Beverages By Using An Acid Urease Column-FIA System"
Talanta 2004 Volume 64, Issue 5 Pages 1278-1282
Y. Iida, M. Ikeda, M. Aoto and I. Satoh

Abstract: An acid urease column was applied to a fluorometric flow-injection analysis (FIA) system as a recognition element for determination of urea in rice wines. The acid urease has specific properties of showing its catalytic activity in low pH range and tolerance to ethanol in comparison to those of a urease from jack-beans. The enzymes were covalently immobilized onto porous glass beads with controlled pore size and then, packed into a small polymer column. The flow-type of the biosensing system was assembled with a sample injection valve, the immobilized enzyme column, and a flow-through quartz cell attached to a fluorescent spectrophotometer. Citrate buffer (50 mM, pH 5.0) as the carrier solution was continuously pumped through the system. Sample solutions were introduced into the system via a rotary injection valve. A standard urea solution was measured through monitoring variations in fluorescent intensity attributable to fluorescent isoindole derivatives formed by coupling with ammonia molecules released in the enzymatic hydrolysis of urea and orthophthalaldehyde reagents. The fluorescent intensity was measured under the conditions of λex = 415 nm and λem = 485 nm. A wide, linear relationship was obtained between the concentration of urea (1.0-100 µM) and the variation in fluorescent intensity. The monitoring did not suffer from ethanol and various amino acids contained in rice wines. Real samples pretreated with ion exchange resins for removal of endogenous ammonia were introduced into the FIA system and urea in the samples was determined. These results were compared with those obtained with use of an F-kit method. The proposed FIA system should present sensitive, selective and convenient analysis of urea in alcoholic beverages.

"Electrochemical Enhancement For Flow-amperometric Biosensing With An Oxidase Column"
Sens. Actuat. B 2003 Volume 91, Issue 1-3 Pages 175-179
Yasuhiro Iida, Takuya Kikuchi and Ikuo Satoh

Abstract: An electrolytic device to enlarge a determination range for biosensing with use of oxidase was fabricated and introduced into a flow-injection amperometric system for Image-ascorbate. The biosensing system was assembled with the plunger pump, the electrolytic device, an immobilized laccase column unit, a flow-through type of oxygen electrode and a pen recorder. The electrolytic device enabled to increase dissolved oxygen in the flow streams by electrolysis of the carrier, and thereby, the additional oxygen attributable to electrolysis should be provided to the laccase column and contribute an activation of the laccase reaction. Image-Ascorbate solutions (20 µl) with various concentrations were injected to the system without the electrolytic device and amounts of dissolved oxygen enzymatically consumed were amperometrically monitored. A linear relationship was obtained in a range of 0.25-4.0 mM. On the other hand, a wider linear range of the Image-ascorbic acid determination was obtained with use of the electrolytic device (0.25-10.0 mM). Not only laccase but other oxidases, such as ascorbate oxidase and glucose oxidase, were immobilized and introduced into this electrolytic FIA system. Determination ranges of the substrates were also enlarged by using the system. This study indicated that use of the electrolytic device enabled to extend the dynamic range of substrate for the oxidases without any mediators.

"Amperometric Sensing System For The Detection Of Urea By A Combination Of The PH-stat Method And Flow Injection Analysis"
Sens. Actuat. B 2001 Volume 76, Issue 1-3 Pages 152-157
Kenji Yoneyama, Yusuke Fujino, Tetsuya Osaka and Ikuo Satoh

Abstract: A new type of amperometric sensing system for urea was constructed based on combining the pH-stat method and the Bow injection analysis (EIA) to solve the problem of potentiometry of dependency on the buffer concentration to the response of urea and moreover to eliminate the response to interfering substances. In the new system, the response to urea was independent of the buffer concentration and the relation between current response and urea concentration became linear. The possibility of automatic operation of this system with a potentiostatic feed back circuit was also confirmed. In this system, the relationship between urea concentration and current response was found to be linear up to 600 µM (=6.0 x 10^-4 mol L-1). Since the sample path was separated from the electrolysis path, no current response of interfering substances such as ascorbic acid and uric acid occurred at the physiological level. Thus, the possibility of amperometric sensing of urea which has a merit of no dependency on the buffer concentration and moreover no influence of interfering substances was demonstrated.

"Multi-ion Biosensor With Use Of A Hybrid-enzyme Membrane"
Sens. Actuat. B 1995 Volume 24, Issue 1-3 Pages 103-106
Ikuo Satoh* and Yukio Iijima

Abstract: The sensor was based on alkaline phosphatase and ascorbate oxidase co-immobilized on a partially-aminated polyacrylonitrile membrane and was used for recognition of Zn(II), Co(II) and Cu(II). The membrane was attached to a flow-through oxygen electrode for monitoring enzymatic activity. The amperometric flow injection system was as described earlier (Ibid., 1993, B13-14, 162). The carrier solution was 0.1 M Tris hydrochloride buffer of pH 8 containing 1 M NaCl (1 ml/min). Chelating reagents (20 mM 2,6-pyridine dicarboxylate of pH 6 containing 1 M NaCl and 5 mM NN-diethyldithiocarbamate of pH 8) were used to remove Zn(II), Co(II) and Cu(II) where necessary. Cu(II) ions could be determined in the range 0.05-1 mM, Zn(II) in the range 2-200 µM and Co(II) in the range 0.05-1 mM.
Cobalt Copper Zinc Amperometry Sensor Electrode Multidetection Chelation Masking agent

"Calorimetric Flow Injection Determination Of Glutathione With Enzyme - Thermistor Detector"
Sens. Actuat. B 1991 Volume 5, Issue 1-4 Pages 245-247
Ikuo Satoh*, Shuji Arakawa and Akira Okamoto

Abstract: For the cited determination glutathione sulfhydryl oxidase and catalase were immobilized separately with bovine serum albumin on Eupergit-C (100 to 200 µm) and double layered into a small polymer column. Sample solution was introduced at 1 mL min-1 via McIlvain buffer (pH 5.0) and the heat generated was measured by the enzyme - thermistor device. The calibration graph was rectilinear from 0.5 to 10 mM glutathione. Analysis time was 6 min and the coefficient of variation for 5.0 mM glutathione was 1.2% (n = 5).
Glutathione Calorimetry Thermistor Buffer Column Detector Immobilized enzyme

"Analytical Application Of Immobilized Acid Urease For Urea In Flow Streams"
Sens. Actuat. B 1991 Volume 5, Issue 1-4 Pages 241-243
Ikuo Satoh* and Masashi Akahane, Kunio Matsumoto

Abstract: A description is given of a system for the calorimetric flow injection determination of urea (I) which is based on acid urease immobilized on porous glass beads packed into a small polymer column. For determination of I, sample is introduced at 1 mL min-1 via a citrate buffer carrier stream (0.1M; pH 5) and the heat generated by the enzymatic hydrolysis of I is monitored through the enzyme thermistor system. The calibration graph was rectilinear from 0.05 to 2 mM I (1 mL samples). Analysis time was 6 min and the coefficient of variation for 1.0 mM I was 1%. The method may be applied to the determination of I in alcoholic beverages.
Urea Calorimetry Thermistor Buffer Column Immobilized enzyme Porous glass beads

"Amperometric Biosensing Of Copper(II) Ions With An Immobilized Apoenzyme Reactor"
Sens. Actuat. B 1990 Volume 1, Issue 1-6 Pages 499-503
Ikuo Satoh*, Teruo Kasahara and Naoto Goi

Abstract: An amperometric flow injection system, incorporating an immobilized-apoenzyme reactor for specific recognition of Cu, is presented (diagram given). Copper ions were selectively determined in the range 0.1 to 10 mM by activation of immobilized metal-free galactose oxidase (I). The I was immobilized on alkylamino controlled pore glass beads (120 to 200 mesh; pore diameter 51.5 nm) and the preparation was loaded into a plastic column which was mounted in a water-jacketed holder. A polarographic O electrode, or a cellulose-acetate-membrane covered Pt - Ag - AgCl electrode pair, housed in a plastic flow-through cell was connected to the outlet of the enzyme reactor to monitor the amount of O consumed, or H2O2 generated, by the activated enzyme. A constant voltage of -0.7 V vs. Ag - AgCl for O, or 0.7 V vs. Ag - AgCl for H2O2, was applied to the Pt electrode. The carrier solution (1 mL min-1) was 0.05 M phosphate buffer (pH 6) containing 0.1 M KCl. D-Galactose solution was added as substrate solution and 10 mM N,N-diethyldithiocarbamate solution (pH 8) was used to regenerate the reactor.
Copper(II) Amperometry Electrode Sensor Immobilized enzyme Controlled pore glass Glass beads pH Buffer

"Flow Injection Calorimetry Of Heavy Metal Ions Using Apoenzyme-reactors"
Netsu Sokutei 1991 Volume 18, Issue 2 Pages 89-96
I.Satoh

Abstract: A review is presented, with 32 references.
Metals, heavy Calorimetry Enzyme Reactor Review

"Flow Injection Micro-determination Of Heavy Metal Ions Using A Column Packed With Immobilized Apoenzyme Beads"
J. Flow Injection Anal. 1991 Volume 8, Issue 2 Pages 111-126
IKUO SATOH

Abstract: A review is presented, with 25 references, in which the principle and characteristics as well as assay procedures for Zn, Cu(II) and Co(II) determination are described. A novel idea for biochemical microanalysis of heavy metal ions in combination with flow-injection techniques is proposed. The microdetermination of the cofactors based on an apoenzyme reactivation method is reviewed exemplifying the assays for heavy metal ions with use of several kinds of immobilized metalloenzymes as the recognition elements for each metal ion.
Cobalt(II) Copper(II) Zinc Column Immobilized enzyme Review

"Application Of An Electrolytic Device To An FIA System For Extension Of The Determination Range Of L-ascorbic Acid"
Electrochemistry 2002 Volume 70, Issue 7 Pages 515-517
Yasuhiro IIDA, Takuto SATOH, Ikuo SATOH

Abstract: The flow injection amperometric determination of L-ascorbic acid with a laccase column was investigated. Laccase (EC 1. 10. 3. 1.) covalently immobilized onto porous glass beads was used as a recognition element for L-ascorbic acid. The immobilized enzymes were packed into a small polymer column, and then mounted in a water-jacketed holder. The biosensing system was assembled with the column unit and a flow-through type of an oxygen electrode for monitoring dissolved oxygen enzymatically consumed. L-Ascorbic acid was amperometrically determined in a range of 0. 05-1.0 mM. In order to increase the amount of dissolved oxygen in the carrier stream, an electrolytic device was applied to the FIA system. Then, we could expand the linear range of the L-ascorbic acid determination from 0.05 to 2.0 mM by using the electrolytic device.

"An Apoenzyme Thermistor Microanalysis For Zinc(II) Ions With Use Of An Immobilized Alkaline Phosphatase Reactor In A Flow System"
Biosens. Bioelectron. 1991 Volume 6, Issue 4 Pages 375-379
Ikuo Satoh

Abstract: Calorimetric microdetermination of zinc(II) ions with use of an apoenzyme thermistor in a flow stream is proposed. Alkaline phosphatase as the selective recognition element was immobilized onto oxirane-acrylic beads (Eupergit-C) and packed into a small polymer column. The flow injection biosensing system was assembled with the immobilized enzyme reactor and a thermistor device for monitoring the enzyme activity. Zinc(II) ions were calorimetrically determined in the range 0.01-1.0 mM for 0.5 mL samples through their activation of the immobilized metal-free alkaline phosphatase (apoenzyme) reactor. The activity of the reactor was assessed by injecting 0.1 mL of 100 mM p-nitrophenyl phosphate solution. Regeneration of the reactor was performed by pumping 20 mM 2.6-pyridine dicarboxylate (pH 6.0) between successive samples. The system could be repeatedly used at least 120 times during 2 months of operation.
Zinc(II) Calorimetry Thermistor Immobilized enzyme Column

"Use Of A Laccase-column For Flow-injection Calorimetry"
Ann. NY Acad. Sci. 1998 Volume 864, Issue 12 Pages 493-496
Ikuo Satoh, Ikuko Sakurai

Abstract: A great number of enzyme-catalyzed reactions are accompanied by heat evolutions.1 Therefore, flow-injection analysis (FIA) based on calorimetry, that is, flow-injection calorimetry,2,3 in combination with biocatalysts as specific recognition elements gives convenient and versatile analytical methods for biorelated compounds. Nakatani and Shimizu purified a thermostable laccase from Trametes sp. and reported its enzymatic properties recently.4 The enzyme functioned as the catalyst in oxidative reactions of various kinds of dihydroxylated compounds (so-called polyphenol compounds). We tried to apply its enzymatic properties to the determination of L-ascorbate in soft drinks. In this paper, we describe the fundamental performance of the calorimetric FIA system with use of the enzymes immobilized onto porous glass beads.
Ascorbate Soft drink Calorimetry Immobilized enzyme Controlled pore glass